Immobilization of the periplasmic maltose-binding protein of Escherichia coli.
Easy and rapid procedures for immobilization of the periplasmic maltose-binding protein was worked out. The matrix was able to adsorb a maltose-chemosensing component, methyl-accepting chemotaxis protein of tar pathway. The adsorption was not seriously affected by the presence of other chemicals in tar pathway such as aspartate or nickel ion.
D018528:ATP-Binding Cassette Transporters; D000327:Adsorption; D001224:Aspartic Acid; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000302:isolation & purification*; D004926:Escherichia coli / Q000032:analysis*; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D009532:Nickel; D033902:Periplasmic Binding Proteins; D012694:Serine
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C461619:MalE protein, E coli; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C461599:maltose transport system, E coli; D001224:Aspartic Acid; D012694:Serine; D009532:Nickel